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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: E3 ubiquitin-protein ligase RING1

UniprotKB/SwissProt ID: Q06587 (Q06587)

Gene Name: RING1

Organism: Homo sapiens (Human)

Function: Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Nucleus speckle

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR032443 RAWUL
IPR043540 RING1/RING2
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

The S-nitrosylation sites of Q06587

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 398 FWKVSRPLEL C YAPTKDPK--  CCCCCCCCCH H HHEEEEEEEC  1.67% 19483679
2 72 KECLHRFCSD C IVTALRSGNK  CCCCCCCCCH H HHEEEEEEEC  1.23%